Linked Life Data

7929039

Source:http://linkedlifedata.com/resource/pubmed/id/7929039

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
1994-10-27
pubmed:abstractText
Affinities of long chain fatty acids (FA) for fatty acid-binding proteins (FABPs) have been measured by monitoring the concentrations of the unbound or free fatty acids (FFA) in equilibrium with the FABPs using the fluorescent probe ADIFAB. This probe allows the measurement of the concentration of FFA in equilibrium with FABPs, without physical separation of any of the reactants. Equilibrium characteristics were measured at 37 degrees C for palmitate, stearate, oleate, linoleate, linolenate, and arachidonate binding to six FABPs from intestine, heart, adipose, and liver from different species. Equilibrium constants for each FA were found to be extremely sensitive to the tissue origin of the FABP but largely independent of species differences. The measured values of the dissociation constants (Kd) ranged from about 2 to 1000 nM, depending upon the tissue origin of the FABP and the FA. Binding constants for some FABPs varied considerably with different FA, as much as 80-fold in the case of the intestinal FABP. In contrast, Kd values for adipocyte FABPs exhibited less than 4-fold variation with FA type and are generally larger (lower affinities) than for the other FABPs. For all FABPs, Kd values for fatty acids with the same chain length were considerably lower for saturated as compared to polyunsaturated FA. This characteristic likely reflects the lower aqueous solubilities of the saturated fatty acids. In contrast to the other FABPs, rat liver FABP was found to have two FA-binding sites/monomer. Each of these two sites had similar high affinities for the saturated FA, while for the unsaturated FA the two sites exhibited affinities that differ by more than 7-fold. This study disagrees with earlier investigations in finding that equilibrium binding of FA to FABPs is a sensitive function of FA type and FABP tissue origin and that FA-FABP dissociation constants are submicromolar. These results provide a framework with which to understand better the biological function of FABPs and the FA-FABP interaction.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/FABP7 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fabp5 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fabp7 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Fabp7 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acid-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/acrylodated intestinal fatty acid...
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23918-30
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Equilibrium constants for the binding of fatty acids with fatty acid-binding proteins from adipocyte, intestine, heart, and liver measured with the fluorescent probe ADIFAB.
pubmed:affiliation
Medical Biology Institute, La Jolla, California 92037.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.